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[[Image:1usl.jpg|left|200px]]
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{{STRUCTURE_1usl|  PDB=1usl  |  SCENE=  }}
'''STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE.'''


==Structure Of Mycobacterium tuberculosis Ribose-5-Phosphate Isomerase, RpiB, Rv2465c, Complexed With Phosphate.==
<StructureSection load='1usl' size='340' side='right'caption='[[1usl]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1usl]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1usl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usl OCA], [https://pdbe.org/1usl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usl RCSB], [https://www.ebi.ac.uk/pdbsum/1usl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPIB_MYCTU RPIB_MYCTU] Has isomerase activity towards D-ribose 5-phosphate, but not towards D-allose 6-phosphate.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/us/1usl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1usl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the synthesis of ribose from other sugars, as well a means for salvage of carbohydrates after nucleotide breakdown. Two unrelated types of enzyme are known to catalyze the isomerization. The most common one, RpiA, is present in almost all organisms. The second type, RpiB, is found in many bacterial species.Here, we demonstrate that the RpiB from Mycobacterium tuberculosis (Rv2465c) has catalytic properties very similar to those previously reported for the Escherichia coli RpiB enzyme. Further, we report the structure of the mycobacterial enzyme, solved by molecular replacement and refined to 1.88A resolution. Comparison with the E.coli structure shows that there are important differences in the two active sites, including a change in the position and nature of the catalytic base. Sequence comparisons reveal that the M.tuberculosis and E.coli RpiB enzymes are in fact representative of two distinct sub-families. The mycobacterial enzyme represents a type found only in actinobacteria, while the enzyme from E.coli is typical of that seen in many other bacterial proteomes. Both RpiBs are very different from RpiA in structure as well as in the construction of the active site. Docking studies allow additional insights into the reactions of all three enzymes, and show that many features of the mechanism are preserved despite the different catalytic components.


==Overview==
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site.,Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL J Mol Biol. 2004 Jan 16;335(3):799-809. PMID:14687575<ref>PMID:14687575</ref>
Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the synthesis of ribose from other sugars, as well a means for salvage of carbohydrates after nucleotide breakdown. Two unrelated types of enzyme are known to catalyze the isomerization. The most common one, RpiA, is present in almost all organisms. The second type, RpiB, is found in many bacterial species.Here, we demonstrate that the RpiB from Mycobacterium tuberculosis (Rv2465c) has catalytic properties very similar to those previously reported for the Escherichia coli RpiB enzyme. Further, we report the structure of the mycobacterial enzyme, solved by molecular replacement and refined to 1.88A resolution. Comparison with the E.coli structure shows that there are important differences in the two active sites, including a change in the position and nature of the catalytic base. Sequence comparisons reveal that the M.tuberculosis and E.coli RpiB enzymes are in fact representative of two distinct sub-families. The mycobacterial enzyme represents a type found only in actinobacteria, while the enzyme from E.coli is typical of that seen in many other bacterial proteomes. Both RpiBs are very different from RpiA in structure as well as in the construction of the active site. Docking studies allow additional insights into the reactions of all three enzymes, and show that many features of the mechanism are preserved despite the different catalytic components.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1USL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USL OCA].
</div>
<div class="pdbe-citations 1usl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site., Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL, J Mol Biol. 2004 Jan 16;335(3):799-809. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14687575 14687575]
*[[Ribose-5-phosphate isomerase 3D structures|Ribose-5-phosphate isomerase 3D structures]]
[[Category: Mycobacterium tuberculosis]]
== References ==
[[Category: Ribose-5-phosphate isomerase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Andersson, C E.]]
</StructureSection>
[[Category: Jones, T A.]]
[[Category: Large Structures]]
[[Category: Mowbray, S L.]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Roos, A K.]]
[[Category: Andersson CE]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Jones TA]]
[[Category: Unge, T.]]
[[Category: Mowbray SL]]
[[Category: Isomerase]]
[[Category: Roos AK]]
[[Category: Pentose phosphate pathway]]
[[Category: Unge T]]
[[Category: Phosphopentose isomerase b]]
[[Category: Phosphoriboisomerase b]]
[[Category: Rv2465c]]
[[Category: Spine]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
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